Lipoprotein lipase: structure, function, regulation, and role in disease

J Mol Med (Berl). 2002 Dec;80(12):753-69. doi: 10.1007/s00109-002-0384-9. Epub 2002 Oct 24.


Lipoprotein lipase (LPL) catalyses the hydrolysis of the triacylglycerol component of circulating chylomicrons and very low density lipoproteins, thereby providing non-esterified fatty acids and 2-monoacylglycerol for tissue utilisation. Research carried out over the past two decades have not only established a central role for LPL in the overall lipid metabolism and transport but have also identified additional, non-catalytic functions of the enzyme. Furthermore, abnormalities in LPL function have been found to be associated with a number of pathophysiological conditions, including atherosclerosis, chylomicronaemia, obesity, Alzheimer's disease, and dyslipidaemia associated with diabetes, insulin resistance, and infection. Advances have also been made in relating the various domains in the protein to different functions, and in understanding the mechanisms that are responsible for the changes in LPL expression seen in response to nutritional and other physiological changes, and during disease. This review summarises recent findings in relation to the structure, function, and regulation of LPL along with its important role in disease.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Arteriosclerosis / genetics
  • Gene Expression Regulation*
  • Humans
  • Lipoprotein Lipase / chemistry*
  • Lipoprotein Lipase / genetics
  • Lipoprotein Lipase / physiology*
  • Lipoproteins / metabolism
  • Mice
  • Models, Biological
  • Obesity / genetics
  • Rats
  • Signal Transduction
  • Structure-Activity Relationship
  • Tissue Distribution


  • Lipoproteins
  • Lipoprotein Lipase